ID E9NX12_WHEAT Unreviewed; 411 AA.
AC E9NX12;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=GDH {ECO:0000313|EMBL:AMP82108.1};
GN ORFNames=CFC21_068137 {ECO:0000313|EMBL:KAF7061441.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EMBL:ADW95819.1};
RN [1] {ECO:0000313|EMBL:ADW95819.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Roots {ECO:0000313|EMBL:ADW95819.1};
RA Grabowska A.;
RT "Isolation and characterization of a cDNA that encodes wheat glutamate
RT dehydrogenase.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMP82108.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:AMP82108.1};
RA Gayatri, Sinha S.K., Dalal M., Mandal P.K.;
RT "Cloning and sequence analysis of glutamate dehydrogenase gene from bread
RT wheat (Triticum aestivum).";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF7061441.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7061441.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [4] {ECO:0000313|EnsemblPlants:TraesCS5A02G434100.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5A02G434100.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [5] {ECO:0000313|EnsemblPlants:TraesCS5A02G434100.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [6] {ECO:0000313|EMBL:KAF7061441.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7061441.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023525};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023549};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC ECO:0000256|RuleBase:RU004417}.
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DR EMBL; HQ821868; ADW95819.1; -; mRNA.
DR EMBL; KU869729; AMP82108.1; -; mRNA.
DR EMBL; CM022223; KAF7061441.1; -; Genomic_DNA.
DR SMR; E9NX12; -.
DR STRING; 4565.E9NX12; -.
DR EnsemblPlants; TraesCS5A02G434100.1; TraesCS5A02G434100.1; TraesCS5A02G434100.
DR Gramene; TraesCAD_scaffold_028385_01G000500.1; TraesCAD_scaffold_028385_01G000500.1; TraesCAD_scaffold_028385_01G000500.
DR Gramene; TraesCLE_scaffold_050964_01G000200.1; TraesCLE_scaffold_050964_01G000200.1; TraesCLE_scaffold_050964_01G000200.
DR Gramene; TraesCS5A02G434100.1; TraesCS5A02G434100.1; TraesCS5A02G434100.
DR Gramene; TraesCS5A03G1024000.1; TraesCS5A03G1024000.1.CDS; TraesCS5A03G1024000.
DR Gramene; TraesKAR5A01G0375950.1; cds.TraesKAR5A01G0375950.1; TraesKAR5A01G0375950.
DR Gramene; TraesKAR5A01G0375950.2; cds.TraesKAR5A01G0375950.2; TraesKAR5A01G0375950.
DR Gramene; TraesKAR5D01G0360640.2; cds.TraesKAR5D01G0360640.2; TraesKAR5D01G0360640.
DR Gramene; TraesPAR_scaffold_082627_01G000200.1; TraesPAR_scaffold_082627_01G000200.1; TraesPAR_scaffold_082627_01G000200.
DR Gramene; TraesRN5A0101038000.1; TraesRN5A0101038000.1; TraesRN5A0101038000.
DR Gramene; TraesROB_scaffold_027457_01G000500.1; TraesROB_scaffold_027457_01G000500.1; TraesROB_scaffold_027457_01G000500.
DR Gramene; TraesWEE_scaffold_083931_01G000200.1; TraesWEE_scaffold_083931_01G000200.1; TraesWEE_scaffold_083931_01G000200.
DR OMA; FNAYRVQ; -.
DR OrthoDB; 45283at2759; -.
DR Proteomes; UP000019116; Chromosome 5A.
DR Proteomes; UP000815260; Chromosome 5A.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF29; GLUTAMATE DEHYDROGENASE 3-RELATED; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000185; Glu_DH; 1.
DR PRINTS; PR00082; GLFDHDRGNASE.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 2: Evidence at transcript level;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000185-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT DOMAIN 178..408
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 142
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 411 AA; 44239 MW; 70712D741FE50845 CRC64;
MNALAATSRN FKQAAKLLGL DSKLEKSLLI PFREIKVECT IPKDDGTLAS YVGFRVQHDN
ARGPMKGGIR YHHEVDPDEV NALAQLMTWK TAVANIPYGG AKGGIGCSPG DLSISELERL
TRVFTQKIHD LIGIHTDVPA PDMGTNAQTM AWILDEYSKF HGYSPAVVTG KPVDLGGSLG
RDAATGRGVL FATEALLAEH GKGIAGQRFV IQGFGNVGSW AAQLITEAGG KVIAISDVTG
AVKNSNGIDI AKLMKHSAEN RGIKGFDGGD AVDPTSLLTE ECDVLIPAAL GGVINKDNAD
AIKAKYIIEA ANHPTDPEAD EILAKKGVLI LPDILANSGG VTVSYFEWVQ NIQGFMWDEE
KVNRELKTYM TRAFRDTKEM CRSHHCDLRM GAFTLGVNRV ARATVLRGWE A
//
